title: AFM study of morphology and mechanical properties of a chimeric spider silk and bone sialoprotein protein for bone regeneration.
abstract: Atomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6mer+BSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the chimeric silk protein, 6mer+BSP, and control films consisting of only the silk component (6mer). The behavior of the 6mer+BSP and 6mer proteins in aqueous solution in the presence of calcium (Ca) ions was also assessed to determine interactions between the inorganic and organic components related to bone interactions, anchoring, and biomaterial network formation. The results demonstrated the formation of protein networks in the presence of Ca(2+) ions, characteristics that may be important in the context of controlling materials assembly and properties related to bone formation with this new chimeric silk-BSP protein.
authors.affiliation: Department of Polymer Engineering, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, Guimarães, Portugal.
authors.forename: Sílvia
authors.initials: S
authors.lastname: Gomes
authors.forename: Keiji
authors.initials: K
authors.lastname: Numata
authors.forename: Isabel B
authors.initials: IB
authors.lastname: Leonor
authors.forename: João F
authors.initials: JF
authors.lastname: Mano
authors.forename: Rui L
authors.initials: RL
authors.lastname: Reis
authors.forename: David L
authors.initials: DL
authors.lastname: Kaplan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001672:Biocompatible Materials; D001861:Bone Regeneration; D001842:Bone and Bones / Q000737:chemistry*; D002942:Circular Dichroism; D003001:Cloning, Molecular; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D012795:Sialoglycoproteins / Q000737:chemistry* / Q000235:genetics; D047011:Silk / Q000737:chemistry*; D013112:Spiders
chemical_list: D001672:Biocompatible Materials; D011993:Recombinant Fusion Proteins; D012795:Sialoglycoproteins; D047011:Silk